Étude moléculaire in vitro du mode d'action de peptides bioactifs issus de protéines de lait bovin : peptides inhibiteurs de l'enzyme de conversion de l'angiotensine I et caseinophosphopeptides chélateurs de minéraux

Abstract : Bovine milk proteins are the most important source of bioactive peptides. These peptides may contribute to maintain optimal health state. In the current study, we attempted to elucidate in vitro the molecular interaction mode between both angiotensin I-converting enzyme (ACE) inhibitory peptides and mineral-chelating caseinophosphopeptides (CPP). Indeed, ACE inhibitory peptides from food may provide a natural and safe alternative to prevent hypertension. In order to better understand the relationship between the sequence of ACE inhibitory peptides and their inhibitory potency, the inhibition parameters of rabbit lung somatic ACE (that possesses 2 domains, N and C, which are both catalytically active) by bovine milk peptides (FALPQYLK, FALPQY, ALPMHIR, IPP, and VPP) and other peptides with related sequence were investigated. Moreover, the interaction between some peptides and their derivatives with human somatic ACE was analyzed by Biacore® technology. The mapping of FALPQY-ACE interaction sites in competition with captopril (a competitive inhibitor for both sites) and also with BPP-11b (a selective inhibitor of the C-domain active site) showed that FALPQY binds at or near the two active sites located on the 2 domains of ACE. In addition, CPP efficiently bind cations of nutritional interest by forming soluble complexes which prevent the precipitation of minerals at alkaline pH and increasing thus their bioavailability. The interaction between [beta]-CN (f1-25)4P, and Ca2+, Mg2+, Zn2+, and Cu2+ cations, was characterized by isothermal titration calorimetry: 1 mole of [beta]-CN (f1-25)4P binds 2 moles of Ca2+, Mg2+, and Zn2+ at a pH 8, with a low affinity, but does not bind Cu2+ cation
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Theses
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http://docnum.univ-lorraine.fr/prive/DDOC_T_2012_0301_ZIDANE.pdf
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https://hal.univ-lorraine.fr/tel-01749473
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Submitted on : Thursday, March 29, 2018 - 12:17:15 PM
Last modification on : Friday, March 30, 2018 - 1:32:24 AM

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  • HAL Id : tel-01749473, version 1

Citation

Faïza Zidane. Étude moléculaire in vitro du mode d'action de peptides bioactifs issus de protéines de lait bovin : peptides inhibiteurs de l'enzyme de conversion de l'angiotensine I et caseinophosphopeptides chélateurs de minéraux. Alimentation et Nutrition. Université de Lorraine, 2012. Français. ⟨NNT : 2012LORR0301⟩. ⟨tel-01749473⟩

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